Structural highlights
Function
[PNAE_RAUSE] Catalyzes the hydrolysis of polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of the ajmaline.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.
Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids.,Yang L, Hill M, Wang M, Panjikar S, Stockigt J Angew Chem Int Ed Engl. 2009;48(28):5211-3. PMID:19496101[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dogru E, Warzecha H, Seibel F, Haebel S, Lottspeich F, Stockigt J. The gene encoding polyneuridine aldehyde esterase of monoterpenoid indole alkaloid biosynthesis in plants is an ortholog of the alpha/betahydrolase super family. Eur J Biochem. 2000 Mar;267(5):1397-406. PMID:10691977
- ↑ Yang L, Hill M, Wang M, Panjikar S, Stockigt J. Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids. Angew Chem Int Ed Engl. 2009;48(28):5211-3. PMID:19496101 doi:10.1002/anie.200900150
